The Mtm1p carrier and pyridoxal 5′-phosphate cofactor trafficking in yeast mitochondria
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چکیده
منابع مشابه
Binding of Pyridoxal 5'-Phosphate
1. The a and ,B subforms of aspartate aminotransferase were purified from pig heart. 2. The a subform contained 2mol of pyridoxal 5'-phosphate. The apo-(a subform) could be fully reactived by combination with 2mol of cofactor. 3. The protein fluorescence of the apo(a subform) decreased non-linearly with increase in enzyme activity and concentration of bound cofactor. 4. It is concluded that the...
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Pyridoxal 5•L-phosphate (PLP) is known to combine with bovine serum albumin to form a(1:1) complex which scarcely dissociates, even when subjected to intensive dialysis. When this complex was incubated with apo-aspartate aminotransferase (apoGOT) for an appropriate time and the preincubated mixture then submitted to the usual GOT assay, the appearance of GOT activity was obviously confirmed, in...
متن کاملTransport of pyridoxine and pyridoxal 5'-phosphate in isolated rat liver mitochondria.
The transport of [14C]pyridoxal-P and [14C]pyridoxine into isolated rat mitochondria was studied by centrifugal filtration. The incubation medium contained 20 mM 2-oxoglutarate and 10 mM inorganic phosphate to inhibit metabolism of pyridoxal-P by the mitochondria. The ratio of [14C]pyridoxine space to [3H]H2O space rapidly attained unity independent of the [14C]pyridoxine concentration in the m...
متن کاملOn the reactivity of pyridoxal-5'-phosphate with yeast tRNAPhe and tRNATyr.
Yeast tRNAPhe and tRNATyr were reacted with the fluorescent reagent pyridoxal-5'-phosphate and the modified tRNAs were analysed with respect to the number and position of modified nucleosides and with respect to aminoacylation. a) Following the intrinsic fluorescence of pyridoxal-5'-phosphate, the treatment of tRNATyr with increasing amounts of pyridoxal-5'-phosphate revealed about 50 mol or re...
متن کاملPyridoxal 5”Phosphate-dependent Histidine Decarboxylase
Pyridoxal phosphate-dependent histidine decarboxylase from Morganella morganii AM-15 was inactivated by (a-a-fluoromethylhistidine by a pseudo firstorder reaction, with KI and kinact values of 0 . 1 mM and 32.2 min-l, respectively, and was most efficient at pH 6.5-7.0. Both L-histidine and the competitive inhibitor, L-histidine methyl ester, protected against inactivation. The apoenzyme was not...
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ژورنال
عنوان ژورنال: Archives of Biochemistry and Biophysics
سال: 2015
ISSN: 0003-9861
DOI: 10.1016/j.abb.2015.01.021